| identifier: | 1772912 |
| description: |
epitope description:P1390, Q1391, R1392, S1394, R1395, N1396, F1397, V1398, R1399, N1421, K1423, Q1424, L1427
antigen name:von Willebrand factor
host organism:Mus musculus
antibody name:NMC-4
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
9501911 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/496 |
| landingPage: |
http://www.iedb.org/assay/1772912 |
| type: |
Literature
|
| publicationVenue: |
Nat Struct Biol
|
| dates: |
1998
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
R Celikel
K I Varughese
Madhusudan
A Yoshioka
J Ware
Z M Ruggeri
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| method: |
ELISA
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| name: |
Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab.
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| description: |
Epitope residues were calculated from the structure [PDB: 1OAK] as the antigen residues interacting with the antibody fragment at atomic distance of 4 Å
. Mapping of residue numbers between PDB and GenBank was done as provided in PDB.
Epitope specific Fab NMC-4 bound to the vWF A1 domain. A1 domain mutants with Arg632 or Arg636 replaced by Ala do not bind Fab NMC-4, confirming their importance as antibody contact residues. The mutations did not affect A1 domain binding to GP Ibalpha under blood flow conditions.
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| name: |
iedb
|
| homePage: |
http://www.iedb.org |